1tzp | pdb_00001tzp
MEPA, inactive form without ZN in P21
Structural highlights
Function[MEPA_ECOLI] Involved in the removal of murein from the sacculus. May also facilitate integration of nascent murein strands into the sacculus by cleaving the peptide bonds between neighboring strands in mature murein.[1] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedLAS enzymes are a group of metallopeptidases that share an active site architecture and a core folding motif and have been named according to the group members lysostaphin, D-Ala-D-Ala carboxypeptidase and sonic hedgehog. Escherichia coli MepA is a periplasmic, penicillin-insensitive murein endopeptidase that cleaves the D-alanyl-meso-2,6-diamino-pimelyl amide bond in E. coli peptidoglycan. The enzyme lacks sequence similarity with other peptidases, and is currently classified as a peptidase of unknown fold and catalytic class in all major data bases. Here, we build on our observation that two motifs, characteristic of the newly described LAS group of metallopeptidases, are conserved in MepA-type sequences. We demonstrate that recombinant E. coli MepA is sensitive to metal chelators and that mutations in the predicted Zn2+ ligands His-113, Asp-120, and His-211 inactivate the enzyme. Moreover, we present the crystal structure of MepA. The active site of the enzyme is most similar to the active sites of lysostaphin and D-Ala-D-Ala carboxypeptidase, and the fold is most closely related to the N-domain of sonic hedgehog. We conclude that MepA-type peptidases are LAS enzymes. Peptidoglycan amidase MepA is a LAS metallopeptidase.,Marcyjaniak M, Odintsov SG, Sabala I, Bochtler M J Biol Chem. 2004 Oct 15;279(42):43982-9. Epub 2004 Jul 29. PMID:15292190[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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